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. 2009 Apr 3;37(11):3501–3513. doi: 10.1093/nar/gkp218

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© 2009 The Author(s)

This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

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Figure 1. — The pADPr-binding motif in Drosophila Hrp38 and Squid protein. (A) Conserved functional domains of Drosophila hrp38 protein. RBD: RNA-binding domains. RGG: glycine-rich domain. M9: nuclear shuttling signal domain. (B) Alignment of putative pADPr-binding sequences of human and Drosophila hnRNPs with the consensus of pADPr-binding motif. The conserved residues in the pADPr-binding motif among human hnRNP A1, hrp38 and Squid are marked in red; among human hnRNP M and Drosophila Squid, they are marked in blue (b: basic, h: hydrophobic amino acid). (C) The accumulation of pADPr in the puffs. Drosophila polytene chromosomes of the wild-type line (y,w) were immunostained with the anti-pADPr antibody (10H). pADPr: green; DNA: red. (D) The localization of Squid in the puffs. Drosophila polytene chromosomes of the wild-type line (y,w) were immunostained with the anti-Squid antibody. Squid: green; DNA: red. Arrows in (C) and (D) indicate the E74 and E75 puffs.